Balancing multiple objectives in conformation sampling to control decoy diversity in template-free protein structure prediction.

ABSTRACT:

Background

Computational approaches for the determination of biologically-active/native three-dimensional structures of proteins with novel sequences have to handle several challenges. The (conformation) space of possible three-dimensional spatial arrangements of the chain of amino acids that constitute a protein molecule is vast and high-dimensional. Exploration of the conformation spaces is performed in a sampling-based manner and is biased by the internal energy that sums atomic interactions. Even state-of-the-art energy functions that quantify such interactions are inherently inaccurate and associate with protein conformation spaces overly rugged energy surfaces riddled with artifact local minima. The response to these challenges in template-free protein structure prediction is

SUBMITTER: Zaman AB 

PROVIDER: S-EPMC6485169 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature